ID A6EQE9_9BACT Unreviewed; 420 AA.
AC A6EQE9;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=SCB49_05295 {ECO:0000313|EMBL:EDM44418.1};
OS unidentified eubacterium SCB49.
OC Bacteria; Bacteroidota; environmental samples.
OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM44418.1, ECO:0000313|Proteomes:UP000003659};
RN [1] {ECO:0000313|EMBL:EDM44418.1, ECO:0000313|Proteomes:UP000003659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM44418.1,
RC ECO:0000313|Proteomes:UP000003659};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDM44418.1}.
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DR EMBL; ABCO01000004; EDM44418.1; -; Genomic_DNA.
DR AlphaFoldDB; A6EQE9; -.
DR STRING; 50743.SCB49_05295; -.
DR Proteomes; UP000003659; Unassembled WGS sequence.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000891; PYR_CT.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Reference proteome {ECO:0000313|Proteomes:UP000003659};
KW Transferase {ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 35..296
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 420 AA; 46474 MW; 009BF669CB288EF8 CRC64;
MGIVKHRKPG FSKKYHLINL FENTKLNLKM SNNYIQIFDT TLRDGEQVPG CKLDTKQKVI
IAEQLDLLGV NVIEAGFPVS SPGDFNAVKA VSRVVKNATV CALSRSVKND IKTAAESLEG
AKYPRIHTGI GTSESHIKYK FKTTQEDILE RAFEAVKYAK TFVEDIEFYA EDAGRTNNEY
LARVCEAAIK AGATVLNIPD TTGYCLPSEY GSKIKYLKEH VKGIDNVILS CHCHNDLGLA
TANAIEGIIN GAKQVECTIN GIGERAGNTA LEEVVMVLKQ HPYLNIETQI DTTRLYGISQ
LVSESMGVYT QPNKAIVGVN AFAHSSGIHQ DGIIKNRETY EIINPKDVGV IESSIVLTAR
SGRAALAYRA KNVGYNLTKL QLDNVYENFL HFADKKKEVN NNDIHQIIET SKVYQEIKTN
//
